ID   CAPSD_HASV7             Reviewed;         791 AA.
AC   Q96818;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 2.
DT   02-JUN-2021, entry version 49.
DE   RecName: Full=Capsid polyprotein VP90;
DE   Contains:
DE     RecName: Full=Capsid polyprotein VP70;
DE   Contains:
DE     RecName: Full=Capsid protein VP34;
DE   Contains:
DE     RecName: Full=Capsid protein VP27;
DE   Contains:
DE     RecName: Full=Capsid protein VP25;
GN   ORFNames=ORF2;
OS   Human astrovirus-7 (HAstV-7).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Stellavirales; Astroviridae; Mamastrovirus.
OX   NCBI_TaxID=38950;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9170498; DOI=10.1007/s007050050112;
RA   Monceyron C., Grinde B., Jonassen T.O.;
RT   "Molecular characterisation of the 3'-end of the astrovirus genome.";
RL   Arch. Virol. 142:699-706(1997).
CC   -!- FUNCTION: The capsid polyprotein VP90 self-assembles and undergoes a
CC       proteolytic cleavage by host caspases to yield the VP70 virions. This
CC       immature virion is composed of 180 VP70 subunits with 90 dimeric spikes
CC       and displays a T=3 icosahedral symmetry. The mature virion is obtained
CC       by further cleavages resulting in three structural proteins VP25, VP27
CC       and VP34. This forms contains only 30 spikes located on the icosahedral
CC       2-fold axes. Plays a role in the attachment to target host cell. This
CC       attachment induces virion internalization through clathrin-dependent
CC       endocytosis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature protein(s). VP90
CC       acidic C-terminal domain is eliminated from the immature virion by host
CC       caspases during viral maturation giving rise to virions composed of
CC       VP70. Further tryptic cleavages occur resulting in the three structural
CC       proteins VP34, VP27 and VP25 and confering infectivity (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the astroviridae capsid polyprotein family.
CC       {ECO:0000305}.
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DR   EMBL; Y08632; CAA69922.2; -; Genomic_RNA.
DR   SMR; Q96818; -.
DR   PRIDE; Q96818; -.
DR   GO; GO:0039617; C:T=3 icosahedral viral capsid; ISS:UniProtKB.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; ISS:UniProtKB.
DR   Gene3D; 2.60.120.20; -; 1.
DR   InterPro; IPR022027; Astro_capsid_p.
DR   InterPro; IPR004337; Capsid_astroviral.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF03115; Astro_capsid_N; 1.
DR   Pfam; PF12226; Astro_capsid_p; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Clathrin-mediated endocytosis of virus by host;
KW   T=3 icosahedral capsid protein; Viral penetration into host cytoplasm;
KW   Virion; Virus endocytosis by host; Virus entry into host cell.
FT   CHAIN           1..791
FT                   /note="Capsid polyprotein VP90"
FT                   /id="PRO_0000320237"
FT   CHAIN           1..658
FT                   /note="Capsid polyprotein VP70"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419578"
FT   CHAIN           1..314
FT                   /note="Capsid protein VP34"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419579"
FT   CHAIN           395..648
FT                   /note="Capsid protein VP27"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419580"
FT   CHAIN           425..648
FT                   /note="Capsid protein VP25"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000419581"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          677..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..694
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..713
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            314..315
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            394..395
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            424..425
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            648..649
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            658..659
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   791 AA;  86569 MW;  717453DB686269E9 CRC64;
     MASKSDKQVT VEVNNNNGRS RSRSRGRSQS RGRGRSFKIT VNSKNRGRRQ NGRNKLQSNQ
     RVRNIVNKQL RKQGVTGPKP AICQRATATL GTIGSNTSGS TEIEACILLN PVLVKDATGS
     TQFGPVQALG AQYSMWKLKY LNVKLTSMVG SSAVNGTAVR ISLNPTSTPS STSWSGLGAR
     KHLDVTVGKN AVFRLKPADL GGPRDGWWLT NTNDNASDTL GPSIEIHTLG KTMSSYLNQQ
     FTGGLFLVEL ASEWCFTGYA ANPNLVNLMK STDKQVNVSF EGDNGTPLIM KVPDTSHFAR
     TAVARSSLPT TLARAGQNTT SDTVWQVLNT AVSAAEIVTP PPFNWLIKGG WWFVKLIAGR
     SRAGMRSFYV YPSYQDALSN KPALCTGSVP GGMRVRAAIP TTLQFTQMNQ PSLGHGEVTA
     TLGRSIPTPG DTFKVVLTIG QPLAPNTLNN QTWVNKTTTA PQGQHVVKIA KDTSNYTTMQ
     GFTPISNVTW YTEDFQPSEE PPPISGLQVL VDSRKKADVY AVQQYLNHPS NTKDQLTSIF
     LVKVTTSFQV NNHLSYFYRA AGTGTAVENF KIRGATSEQN ISFSEGWYLM TNTATFNPPA
     PPGWIWKNVE LDNNTPYIVD QGMMHLIMSP PVGTQLLFEM KTTVSGTRNV SHFDHDENPS
     PVWCDALDAA DVWELPTETD TESEEDEDED DEADRFDLHS SYGSEPEDDD ENNRVTLLST
     LINQGMTVER ATMITKRAFP TCADKQKRSV HMDLLASGLS PGNVWSHACE EARTMGTNHM
     PNVSGDRGHA E